cerebral hematoma expansion triggered by intracerebral infusion of autologous blood is increased in diabetic rats, and this response is ameliorated by plasma kallikrein inhibition and deficiency, respectively

while the insertion/deletion angiotensin I-converting enzyme polymorphism affects differently the C- and N-domains as well as the kallikrein-kinin system of young normotensive individuals, this polymorphism can not be associated with effects on handgrip strength

the enzyme drives multiple proteolytic reaction cascades in the cardiovascular system such as the intrinsic pathway of coagulation, the kallikrein-kinin system, the fibrinolytic system, the renin-angiotensin system and the alternative complement pathway

diabetes is associated with increased intrinsic pathway activity, which is mediated in part by plasma kallikrein (PK). PK-mediated activation of the plasminogen cascade is implicated in adipocyte differentiation and adipogenesis during mammary gland involution via activation of plasmin-mediated cleavage of preadipocyte stromal matrix

optimal kallikrein concentration is 5 microg/ml, cleavage of around 70% of neuropeptide Y3-36. Higher concentrations of kallikrein conversely results in a decrease of NPY3-35 levels without an increase of neuropeptide Y3-36 levels, suggesting that high concentrations of kallikrein enable additional and nonspecific neuropeptide Y cleavages

no activity with o-aminobenzoyl-RPGLPVRFESPL-N-(2,4-dinitrophenyl)-ethylene diamine and o-aminobenzoyl-FESPLRINIIKE-N-(2,4-dinitrophenyl)-ethylene diamine, which are based on the Bauhinia bauhinioides inhibitor protein reactive site sequence

the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation

kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview

plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview

the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview

the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview

substrate specificity requirements, very low activity with the equivalent of rat prorenin to the cleavage site and with the peptide o-aminobenzoyl-NVTSPVQ-N-(2,4-dinitrophenyl)-ethylene diamine, activation of rat prorenin requires a different enzyme and/or mechanism

the review indicates how the plasma kallikrein/kinin system and the plasma renin-angiotensin system are activated and interact in endotoxin or related forms of induced sepsis. Activation of both the plasma kallikrein/kinin system and the plasma renin-angiotensin system can lead to increased nitric oxide and prostaglandin formation

kallikrein participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation, it has different specific cellular functions dependent on the tissue, overview

plasma kallikrein activates neutrophil aggregation and degranulation, the enzyme is part of the kallikrein-kininogen-kinin system, KKS, kininogen plays a role in signaling pathways via the kininogen receptors, mechanism of inflammation related to KKS, overview

the enzyme is part of the plasma kallikrein-kininogen-kinin system, PKKS, which is involved in cardiovascular disease and artherothrombosis, e.g. coronary heart disease and stroke in middle-aged men, overview

the enzyme is part of the plasma kallikrein/kinin system that consists of the protein factor XII, prekallikrein, and high-molecular-weight kininogen, intravascular assembly of the plasma kallikrein/kinin system, overview, it acts as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces, kallikrein is involved in development of arterial thrombosis, mechanisms, overview

inhibitor with the best potency and selectivity profile for plasma kallikrein versus related serine proteases. This compound is highly stable in vivo and could be further developed for the treatment and inflammatory or coagulation disorders. Pharmacokinetic data

DX-88 has a strong neuroprotective effect in the early phases of brain ischemia preventing reperfusion injury and indicates that inhibition of plasma kallikrein may be useful tool in the strategy aimed at reducing the detrimental effects linked to reperfusion

ecotin with mutation H53P in the 50s loop, mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop is a high-affinity and highly specific plasma kallikrein inhibitor. Specifically inhibits contact activation of human plasma at the level mediated by plasma kallikrein. Discriminates between enzyme and zymogen. Partial thromboplastin time inhibition can be rescued by addition of PKal

high-molecular weight kininogen is a ferritin-binding protein, binding to the modified light chain of activated kininogen. Binding to kininogen retards the release of bradykinin by inhibition of kallikrein, no inhibition with substrates other than kininogen, binding mechanism, inhibition by holo- and apoferritin

isolation and analysis of the enzyme inhibitor from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ45, recombinant production in insect or Escherichia coli cells, triafestin-1 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview

isolation and analysis of enzyme inhibitors from salivary glands of instar nymphs of Triatoma infestans, SwissProt ID A7BJ46, recombinant production in insect or Escherichia coli cells, triafestin-2 specifically interacts with factor XII and high molecular weight kininogen in a Zn2+-dependent manner, and inhibit activation of the kallikrein-kinin system by interfering with the association of factor XII and high molecular weight kininogen with biological activating surfaces as well as inhibiting prekallikrein activation, overview

activation of plasma kallikrein and generation of bradykinin are responsible for the angioedema attacks observed with C-1 inhibitor deficiency. C1-inhibitor concentration of greater than 0.001 mM is needed to inhibit 3 nM kallikrein

at least four promoter regions and diverse transcription start sites can be utilized. Tissue-dependent alternative use of promoters and transcription starts is evident from a comparison of the start sites in liver and kidney

at least four promoter regions and diverse transcription start sites can be utilized. Tissue-dependent alternative use of promoters and transcription starts is evident from a comparison of the start sites in liver and kidney

x * 52000 + x * 35000, the purified sample exhibits several bands on SDS-PAGE, and the most intense band is found to be the 52000 Da N-terminal subunit of kallikrein by mass spectrometric analysis, two other minor bands around 35000 Da are both C-terminal subunits of kallikrein

the plasma kallikrein/kinin system has two mechanisms for its activation: one that is dependent and another independent of factor XII, the latter is realized by autoactivation on a negatively charged artificial or biologic surface or by serine protease prolylcarboxypeptidase, a PK activator on endothelial cell surfaces, while factor XIIa performs proteolytic activation of the zymogen prekallikrein, overview

protease domain recombinantly expressed in Pichia pastoris or in the baculovirus/Sf9 system. Structure for the endoglycosidase H-deglycosylated protease domain produced from Pichia pastoris is determined at 1.4 A. Structure for the mutagenically deglycosylated form produced from Sf9 cells is determined at 1.4 A

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Cloned/COMMENTARY

ORGANISM

UNIPROT

LITERATURE

expression of the protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. In the baculovirus/Sf9 system, homogenous, crystallizable, and nonglycosylated protein is expressed after mutagenizing three asparagines to glutamate. The activity of the catalytic domain is similar to that of the full-length protein

DX-88 has a strong neuroprotective effect in the early phases of brain ischemia preventing reperfusion injury and indicates that inhibition of plasma kallikrein may be useful tool in the strategy aimed at reducing the detrimental effects linked to reperfusion